Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts: Gene/Protein Disease Symptom Drug Enzyme Compound   Target Concepts: Gene/Protein Disease Symptom Drug Enzyme Compound

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Query: EC:1.11.1.7 (peroxidase)
65,474 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

A detailed analysis of mammalian cell surface proteins is described by a new two-dimensional polyacrylamide gel electrophoresis technique. The first dimension gel contains 2% acrylamide, 0.1% sodium dodecyl sulfate, 0.3% Triton CF10 and 9 M urea. A combination of the detergents and urea permits the separation of poorly soluble, hydrophobic cell surface proteins. Under these conditions, the molecular size of proteins has a limited contribution to the fianl separation due to a low acrylamide concentration. Differences in charge properties, hydrophobicity, and glycosylation are the elements determining the resolution. In the second dimension, the proteins are separated primarily according to molecular weights, by a conventional polyacrylamide gel system in the presence of 0.1% sodium dodecyl sulfate. In this study, proteins of C6 rat glioma cell line are characterized. Cell surface proteins are specifically radio-labeled with 125I by a lactoperoxidase method, and compared with presumptive integral surface proteins which are resistant to extraction with 0.1 M NaOH. Also studied are total cellular proteins, fucose- and glucosamine-containing glycoproteins, and protein species with variable susceptibility to weak trypsin digestion. The electrophoresis system allows an unambiguous identification of each protein species.
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PMID:A two-dimensional polyacrylamide gel electrophoresis system for the analysis of mammalian cell surface proteins. 700 22

Horseradish peroxidase has been conjugated with human immunoglobulin containing antibody to hepatitis B e antigen (anti-HBe). This was used in a solid-phase 'sandwich' enzyme-linked immunosorbent assay designed for reading by eye, to test sera for HBeAg and anti-HBe. Optimum conditions for preparing the conjugate and for performing the test are described. Results of testing hepatitis B surface antigen (HBsAg)-positive sera were compared with those obtained using a sensitive solid-phase radioimmunoassay. The enzyme assay provided a simple and sensitive method of testing for HBeAg and anti-HBe, and correlated well with the radioimmunoassay.
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PMID:Development of an enzyme-linked immunosorbent assay (ELISA) for hepatitis B e antigen and antibody. 702 74

Immunofixation of sodium lauryl sulphate (SDS)-acrylamide gels has been used to study the distribution of the major protein (clathrin) of coated vesicles in various compartments of synaptic terminals. Synaptosomal subcellular fractions were isolated and purified from pig brain homogenates by the procedure of Ueda et al. and lysed in 6 mM Tris-Cl buffer at pH 6.6, 7.8, and 8.1. The synaptosomal particulate and soluble fractions were separated by centrifugation. The synaptic junctional complex (SJC) and postsynaptic density (PSD) fractions were obtained by detergent treatment of the synaptic plasma membrane (SPM). The synaptosomal subcellular fractions and purified coated vesicle (PCV) fractions were subjected to SDS gel electrophoresis (7.5%). The resulting slabs were divided vertically into 4 segments which were stained with Coomassie blue dye, or immunofixed with preimmune and anti-clathrin serum, or affinity labeled with concanavalin A (Con A)-peroxidase. The Comassie blue stained gel indicated the presence of 180,000-molecular weight band in gels of most synaptosomal subcellular fractions. However, immunofixation of an identical gel revealed positive staining of the 180,000-molecular weight protein in PCV, synaptosomal (SF), SPM and synaptoplasmic (SS) fractions only. These findings not only support the contention that a pool of cytosolic-coated vesicle protein is localized at synaptic terminals, they also indicate that clathrin appears highly unlikely to contribute to the structural frameworks of the SJC and PSD of mature synapses.
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PMID:Compartmentalization of clathrin in synaptic terminals. 709 76

A biochemical system was devised to identify aneuploids of Nicotiana tabacum. Leaf tissue from 6 nullihaploids, 4 nullisomics, and 10 monosomics was analyzed electrophoretically on slab acrylamide gels. The staining systems used were for peroxidase, esterase, superoxide dismutase, malate dehydrogenase, and glutamate oxaloacetate transaminase. Nullihaploids and nullisomics could be distinguished from each other and from haploid or disomic types by their unique isozyme banding patterns. The banding patterns of the monosomics closely resembled those of the disomic. Morphologically similar aneuploids from different populations had similar isozyme banding patterns.
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PMID:Identification of aneuploids in Nicotiana tabacum by isozyme banding patterns. 711 87

The innervation of the caudal neurosecretory system of Poecilia sphenops (black molly) was studied by use of the retrograde horseradish peroxidase (HRP) method. The structure of the caudal neurosecretory system in this species was well suited for application of HRP procedures. Acrylamide/HRP gel implants were placed in the nucleus of the caudal neurosecretory system. Two neuronal groups which contained HRP filled cells were found in the brains tem. Bilateral projections originate from the dorsal tegmentum of the midbrain and the reticular nucleus of the medulla.
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PMID:Brain stem innervation of the caudal neurosecretory system. 717 7

In the F1 hybrids between Durrant's L and Durrant's S flax genotrophs, the relative mobilities of the anionic peroxidase isozymes were essentially the same as those in the L parent. The isozymes in both parents and their F1's were compared over a range of acrylamide gel concentrations, with plots of log relative mobility against gel concentration. Plots of comparative mobility, relative to the internal standard hemoglobin, against concentration were also examined. Both approaches provided evidence that apparent molecular weight modifications underlay the shift in mobility between the parents and the resemblance of the F1's to L, the parent which was homozygous for the dominant alleles controlling the mobility shift for at least two of the isozymes.
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PMID:Molecular weight and net charge of peroxidase isozymes in F1 hybrids between L and S flax genotrophs. 718 51

Previous reports have described conflicting results concerning the glycoprotein (GP) and protein composition of Bernard-Soulier platelets. In view of this controversy we have analyzed the platelets of four Bernard-Soulier patients using improved single and two-dimensional sodium dodecyl sulfate (SDS)-polyacrylamide gel electrophoresis procedures. An absence of staining for carbohydrate of membrane GP Ib was characteristic for the platelets of each patient. Major periodate-Schiff staining bands corresponding to membrane GP IIb, IIIa, and IIIb were clearly detected and their presence was confirmed by two-dimensional SDS-polyacrylamide gel electrophoresis. The protein content of the Bernard-Soulier platelets was increased two- to fourfold. However, analysis of their protein composition using 7-12% acrylamide gradient gels showed normal polypeptide profiles. Lactoperoxidase-catalyzed 125I-labeling of the Bernard-Soulier platelet surface proteins was followed by SDS-polyacrylamide gel electrophoresis and autoradiography. No labeling in the Ib position was detected whereas the other major membrane GP, including Ia and IIa, were normally located. In contrast, GP Ib was clearly detected by periodate-Schiff staining and autoradiography when normal human platelets that had been exhaustively treated with neuraminidase before the lactoperoxidase-catalyzed iodination were analysed. No abnormalities were detected in the GP patterns of membranes isolated from the patients' erythrocytes. Only a severe molecular abnormality or possible deletion of GP Ib could account for this major platelet lesion in the Bernard-Soulier syndrome.
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PMID:Analysis of the glycoprotein and protein composition of Bernard-Soulier platelets by single and two-dimensional sodium dodecyl sulfate-polyacrylamide gel electrophoresis. 722 34

The Fc gamma receptor of rabbit alveolar macrophages was purified by affinity chromatography by using rabbit gamma-globulin (Rab gamma G) coupled to Sepharose. Macrophage preparations were efficiently labeled with 125I by using a modified lactoperoxidase method. After incubation of NP-40 cell lysates with Rab gamma G-Sepharose, elution at 4 degrees C with 0.5 N acetic acid containing 1% NP-40 and rapid neutralization allowed recovery of active Fc gamma receptor. Purified Fc gamma receptor retained its ligand-binding activity, since approximately 41 to 72% of labeled material specifically rebound to Rab gamma G-Sepharose. Active receptor also rebound to human IgG- and rat IgG-sepharose. Active Fc gamma receptor did not bind to Sepharose coupled to rabbit Fab, rabbit F(ab)'2 or human F(ab)'2 fragments, nor to Sepharose coupled to chicken IgG. Analysis of Fc gamma receptor by SDS polyacrylamide gels demonstrated a broad peak of radioactivity in the apparent m.w. range of 50,000 to 70,000 in 5.6% acrylamide gels and 35,000 to 55,000 in 9% gels. Labeled receptor with similar structural characteristics and ligand-binding activity was also obtained from highly purified adherent cell populations and from macrophages biosynthetically-labeled with [14C]glucosamine in culture.
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PMID:Purification of Fc gamma receptor from rabbit alveolar macrophages that retains ligand-binding activity. 737 49

The metabolic fate of cell-surface components was studied by labeling the surface of cultured chick embryo cells with [14C]glucosamine for 24 h, or by lactoperoxidase-catalyzed radioiodination. The cells were then cultured further in label-free medium for 24 h. At different time intervals thereafter, cells and culture medium were subjected to sodium dodecyl sulfate-polyacrylamide gel electrophoresis. The radioactivity profile of the metabolically labeled material in the medium was similar to that of the [125I]lactoperoxidase-labeled cells. The rate of disappearance of labeled macromolecular components from the cell surface was a mirror image of the rate of accumulation of these components in the medium. Analysis on 7 to 20% acrylamide gradient slab gel revealed that most of the labeled macromolecules in the medium comigrate with the surface micromolecules obtained from intact cells. It thus appears that at least some cell-surface components are shed in undegraded form. The possible biomedical implications of the detection of intact cellular membrane components in the circulation are discussed.
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PMID:Cell-surface shedding by fibroblasts in culture. 739 85

Proteins of the stria vascularis of the normal and the genetically deaf waltzing guinea pig were analysed by one and two-dimensional acrylamide gel electrophoresis. Cochlear proteins were labeled in vivo by replacing the perilymph with a solution containing radioactive precursors. With the two-dimensional analysis, more than 200 polypeptides were resolved. Proteins that are exposed on the endolymphatic surface of the stria vascularis were identified by lactoperoxidase-catalysed iodination. Seven polypeptides were identified with this technique. No consistent changes in protein patterns of the stria vascularis from the waltzing guinea pig were detected.
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PMID:Analysis of proteins of the stria vascularis of the normal and the waltzing guinea pig. 744 81


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